TAILIEUCHUNG - Báo cáo khoa học: Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase fromThermus thermophilus

Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase (AK; EC ) fromThermus thermophilus(TtAKb) were deter-mined at A˚ in the Thr-bound form (TtAKb-Thr) and at A ˚ in the Thr-free form (TtAKb-free). Although both forms are crystallized as dimers, the contact surface area of the dimer interface in TtAKb-free (3200 A ˚ 2 ) is smaller than that of TtAKb-Thr (3890 A ˚ 2 ). | Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase from Thermus thermophilus Ayako Yoshida1 Takeo Tomita1 Hidetoshi Kono2 Shinya Fushinobu3 Tomohisa Kuzuyama1 and Makoto Nishiyama1 4 1 Biotechnology Research Center The University of Tokyo Japan 2 ComputationalBiology Group Quantum Beam Science Directorate Japan Atomic Energy Agency Kyoto Japan 3 Department of Biotechnology The University of Tokyo Japan 4 RIKEN SPring-8 Center Hyogo Japan Keywords ACT domain allosteric regulation crystal structure thermostability threonine biosynthesis Correspondence M. Nishiyama Biotechnology Research Center The University of Tokyo 1-1-1 Yayoi Bunkyo-ku Tokyo 113-8657 Japan Fax 81 3 5841 8030 Tel 81 3 5841 3074 E-mail umanis@ Received 3 November 2008 revised 10 March 2009 Accepted 31 March 2009 doi Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase AK EC from Thermus thermophilus TtAKb were determined at A in the Thr-bound form TtAKb-Thr and at A in the Thr-free form TtAKp-l ree . Although both forms are crystallized as dimers the contact surface area of the dimer interface in TtAKp-free 3200 A2 is smaller than that of TtAKp-Thr 3890 A2 . Sedimentation equilibrium analyzed by ultracentrifugation revealed that TtAKb is present in equilibrium between a monomer and dimer and that Thr binding shifts the equilibrium to dimer formation. In the absence of Thr an outward shift of b-strands near the Thr-binding site site 1 and a concomitant loss of the electron density of the loop region between b 3 and b 4 near the Thr-binding site are observed. The mechanism of regulation by Thr is discussed on the basis of the crystal structures. TtAKb has higher thermostability than the regulatory subunit of Corynebacterium glutamicum AK with a difference in denaturation temperature Tm of 40 C. Comparison of the crystal structures of TtAKb and the regulatory subunit of C. .

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